@article{203456,
  keywords = {clathrin-mediated endocytosis, cryo-EM, cryo-ET, dynamin, Endocytosis, membrane fission, membrane remodeling, structural biology},
  author = {John Jimah and Nidhi Kundu and Abigail Stanton and Kem Sochacki and Bertram Canagarajah and Lieza Chan and Marie-Paule Strub and Huaibin Wang and Justin Taraska and Jenny Hinshaw},
  title = {Cryo-EM structures of membrane-bound dynamin in a post-hydrolysis state primed for membrane fission.},
  abstract = {<p>Dynamin assembles as a helical polymer at the neck of budding endocytic vesicles, constricting the underlying\&nbsp;membrane as it progresses through the GTPase cycle to sever vesicles from the plasma\&nbsp;membrane.\&nbsp;Although atomic models of the dynamin helical polymer bound to guanosine triphosphate (GTP) analogs define earlier stages of membrane constriction, there are no atomic models of the\&nbsp;assembled state post-GTP hydrolysis. Here, we used cryo-EM methods to determine atomic structures of the dynamin helical polymer assembled on lipid tubules, akin to necks of budding endocytic vesicles, in a guanosine diphosphate (GDP)-bound, super-constricted state. In this state, dynamin is assembled\&nbsp;as a 2-start helix with an inner lumen of 3.4\&nbsp;nm, primed for spontaneous fission. Additionally, by cryo-electron tomography, we trapped dynamin helical assemblies within HeLa cells using the\&nbsp;GTPase-defective dynamin K44A mutant and observed diverse dynamin helices, demonstrating that dynamin can accommodate a range of assembled complexes in cells that likely precede membrane fission.</p>},
  year = {2024},
  journal = {Developmental cell},
  volume = {59},
  pages = {1783-1793.e5},
  month = {07/2024},
  issn = {1878-1551},
  doi = {10.1016/j.devcel.2024.04.008},
  language = {eng},
}